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Volumn 22, Issue 4, 2014, Pages 515-525

F NMR Reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; NONSTRUCTURAL PROTEIN 1; TRYPTOPHAN; VIRULENCE FACTOR; 5-FLUOROTRYPTOPHAN; PROTEIN BINDING; RECOMBINANT PROTEIN; VIRUS PROTEIN;

EID: 84898459926     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.01.010     Document Type: Article
Times cited : (43)

References (67)
  • 5
    • 84869214374 scopus 로고    scopus 로고
    • Contribution of NS1 effector domain dimerization to influenza A virus replication and virulence
    • J. Ayllon, R.J. Russell, A. García-Sastre, and B.G. Hale Contribution of NS1 effector domain dimerization to influenza A virus replication and virulence J. Virol. 86 2012 13095 13098
    • (2012) J. Virol. , vol.86 , pp. 13095-13098
    • Ayllon, J.1    Russell, R.J.2    García-Sastre, A.3    Hale, B.G.4
  • 6
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • D.D. Boehr, R. Nussinov, and P.E. Wright The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5 2009 789 796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 7
    • 33744925682 scopus 로고    scopus 로고
    • X-ray structure of influenza virus NS1 effector domain
    • Z.A. Bornholdt, and B.V. Prasad X-ray structure of influenza virus NS1 effector domain Nat. Struct. Mol. Biol. 13 2006 559 560
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 559-560
    • Bornholdt, Z.A.1    Prasad, B.V.2
  • 8
    • 57749169511 scopus 로고    scopus 로고
    • X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus
    • Z.A. Bornholdt, and B.V. Prasad X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus Nature 456 2008 985 988
    • (2008) Nature , vol.456 , pp. 985-988
    • Bornholdt, Z.A.1    Prasad, B.V.2
  • 9
    • 77954755663 scopus 로고    scopus 로고
    • Using fluorine nuclear magnetic resonance to probe the interaction of membrane-active peptides with the lipid bilayer
    • B.C. Buer, J. Chugh, H.M. Al-Hashimi, and E.N. Marsh Using fluorine nuclear magnetic resonance to probe the interaction of membrane-active peptides with the lipid bilayer Biochemistry 49 2010 5760 5765
    • (2010) Biochemistry , vol.49 , pp. 5760-5765
    • Buer, B.C.1    Chugh, J.2    Al-Hashimi, H.M.3    Marsh, E.N.4
  • 10
    • 0141569110 scopus 로고    scopus 로고
    • A protein contortionist: Core mutations of GB1 that induce dimerization and domain swapping
    • I.J. Byeon, J.M. Louis, and A.M. Gronenborn A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping J. Mol. Biol. 333 2003 141 152
    • (2003) J. Mol. Biol. , vol.333 , pp. 141-152
    • Byeon, I.J.1    Louis, J.M.2    Gronenborn, A.M.3
  • 11
    • 0002889918 scopus 로고
    • General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation
    • J.P. Carver, and R.E. Richards General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation J. Magn. Reson. 6 1972 89 105
    • (1972) J. Magn. Reson. , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 12
    • 30144444853 scopus 로고    scopus 로고
    • Bioinformatic methods to exploit mass spectrometric data for proteomic applications
    • R.J. Chalkley, K.C. Hansen, and M.A. Baldwin Bioinformatic methods to exploit mass spectrometric data for proteomic applications Methods Enzymol. 402 2005 289 312
    • (2005) Methods Enzymol. , vol.402 , pp. 289-312
    • Chalkley, R.J.1    Hansen, K.C.2    Baldwin, M.A.3
  • 13
    • 59449110919 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition by NS1 protein of influenza A virus
    • A. Cheng, S.M. Wong, and Y.A. Yuan Structural basis for dsRNA recognition by NS1 protein of influenza A virus Cell Res. 19 2009 187 195
    • (2009) Cell Res. , vol.19 , pp. 187-195
    • Cheng, A.1    Wong, S.M.2    Yuan, Y.A.3
  • 20
    • 33846851242 scopus 로고
    • Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance
    • S. Forsén, and R.A. Hoffman Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance J. Chem. Phys. 39 1963 2892 2901
    • (1963) J. Chem. Phys. , vol.39 , pp. 2892-2901
    • Forsén, S.1    Hoffman, R.A.2
  • 22
    • 47749143963 scopus 로고    scopus 로고
    • Structure of an avian influenza A virus NS1 protein effector domain
    • B.G. Hale, W.S. Barclay, R.E. Randall, and R.J. Russell Structure of an avian influenza A virus NS1 protein effector domain Virology 378 2008 1 5
    • (2008) Virology , vol.378 , pp. 1-5
    • Hale, B.G.1    Barclay, W.S.2    Randall, R.E.3    Russell, R.J.4
  • 23
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • B.G. Hale, R.E. Randall, J. Ortín, and D. Jackson The multifunctional NS1 protein of influenza A viruses J. Gen. Virol. 89 2008 2359 2376
    • (2008) J. Gen. Virol. , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortín, J.3    Jackson, D.4
  • 25
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • K. Henzler-Wildman, and D. Kern Dynamic personalities of proteins Nature 450 2007 964 972
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 26
    • 27744480205 scopus 로고    scopus 로고
    • Proteins flex to function
    • Y.J. Huang, and G.T. Montelione Proteins flex to function Nature 438 2005 36 37
    • (2005) Nature , vol.438 , pp. 36-37
    • Huang, Y.J.1    Montelione, G.T.2
  • 27
    • 35348982302 scopus 로고    scopus 로고
    • Stimulation of in vitro sumoylation by Slx5-Slx8: Evidence for a functional interaction with the SUMO pathway
    • T. Ii, J.R. Mullen, C.E. Slagle, and S.J. Brill Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway DNA Repair (Amst.) 6 2007 1679 1691
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1679-1691
    • Ii, T.1    Mullen, J.R.2    Slagle, C.E.3    Brill, S.J.4
  • 28
    • 84861394598 scopus 로고    scopus 로고
    • Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets
    • M. Imai, T. Watanabe, M. Hatta, S.C. Das, M. Ozawa, K. Shinya, G. Zhong, A. Hanson, H. Katsura, and S. Watanabe et al. Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets Nature 486 2012 420 428
    • (2012) Nature , vol.486 , pp. 420-428
    • Imai, M.1    Watanabe, T.2    Hatta, M.3    Das, S.C.4    Ozawa, M.5    Shinya, K.6    Zhong, G.7    Hanson, A.8    Katsura, H.9    Watanabe, S.10
  • 29
    • 84855199911 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of novel small molecule inhibitors of the influenza virus protein NS1
    • J.J. Jablonski, D. Basu, D.A. Engel, and H.M. Geysen Design, synthesis, and evaluation of novel small molecule inhibitors of the influenza virus protein NS1 Bioorg. Med. Chem. 20 2012 487 497
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 487-497
    • Jablonski, J.J.1    Basu, D.2    Engel, D.A.3    Geysen, H.M.4
  • 31
    • 0003060984 scopus 로고
    • Comments on the analysis of sedimentation equilibrium experiments
    • T.M. Schuster, T.M. Laue, Birkhäuser Boston
    • M.L. Johnson, and M. Straume Comments on the analysis of sedimentation equilibrium experiments T.M. Schuster, T.M. Laue, Modern Analytical Ultracentrifugation 1994 Birkhäuser Boston
    • (1994) Modern Analytical Ultracentrifugation
    • Johnson, M.L.1    Straume, M.2
  • 33
    • 0025093242 scopus 로고
    • The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate. Application to fluorotryptophan labelling to the H(+)-ATPase of Escherichia coli and NMR studies
    • H.W. Kim, J.A. Perez, S.J. Ferguson, and I.D. Campbell The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate. Application to fluorotryptophan labelling to the H(+)-ATPase of Escherichia coli and NMR studies FEBS Lett. 272 1990 34 36
    • (1990) FEBS Lett. , vol.272 , pp. 34-36
    • Kim, H.W.1    Perez, J.A.2    Ferguson, S.J.3    Campbell, I.D.4
  • 36
    • 84856520247 scopus 로고    scopus 로고
    • GUARDD: User-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
    • I.R. Kleckner, and M.P. Foster GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data J. Biomol. NMR 52 2012 11 22
    • (2012) J. Biomol. NMR , vol.52 , pp. 11-22
    • Kleckner, I.R.1    Foster, M.P.2
  • 37
    • 84898469114 scopus 로고    scopus 로고
    • The NS1 protein: A master regulator of host and viral functions
    • R.G. Webster, A.S. Monto, T.J. Braciale, R.A. Lamb, John Wiley & Sons Oxford, UK
    • R.M. Krug, and A. Garcia-Sastre The NS1 protein: a master regulator of host and viral functions R.G. Webster, A.S. Monto, T.J. Braciale, R.A. Lamb, Textbook of Influenza 2013 John Wiley & Sons Oxford, UK 114 132
    • (2013) Textbook of Influenza , pp. 114-132
    • Krug, R.M.1    Garcia-Sastre, A.2
  • 38
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S.E. Harding, A.J. Rowe, J.C. Horton, Royal Society of Chemistry Cambridge, UK
    • T.M. Laue, B.D. Shah, T.M. Ridgeway, and S.L. Pelletier Computer-aided interpretation of analytical sedimentation data for proteins S.E. Harding, A.J. Rowe, J.C. Horton, Analytical Ultracentrifugation in Biochemistry and Polymer Science 1992 Royal Society of Chemistry Cambridge, UK 90 125
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 39
    • 79960368594 scopus 로고    scopus 로고
    • Alanine substitutions within a linker region of the influenza A virus non-structural protein 1 alter its subcellular localization and attenuate virus replication
    • W. Li, J.W. Noah, and D.L. Noah Alanine substitutions within a linker region of the influenza A virus non-structural protein 1 alter its subcellular localization and attenuate virus replication J. Gen. Virol. 92 2011 1832 1842
    • (2011) J. Gen. Virol. , vol.92 , pp. 1832-1842
    • Li, W.1    Noah, J.W.2    Noah, D.L.3
  • 42
    • 84862633452 scopus 로고    scopus 로고
    • Dynamics in multi-domain protein recognition of RNA
    • C.D. Mackereth, and M. Sattler Dynamics in multi-domain protein recognition of RNA Curr. Opin. Struct. Biol. 22 2012 287 296
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 287-296
    • Mackereth, C.D.1    Sattler, M.2
  • 44
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • M. Mayer, and B. Meyer Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor J. Am. Chem. Soc. 123 2001 6108 6117
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 45
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: New research developments
    • R.A. Medina, and A. García-Sastre Influenza A viruses: new research developments Nat. Rev. Microbiol. 9 2011 590 603
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 590-603
    • Medina, R.A.1    García-Sastre, A.2
  • 46
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • T. Mittag, L.E. Kay, and J.D. Forman-Kay Protein dynamics and conformational disorder in molecular recognition J. Mol. Recognit. 23 2010 105 116
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 47
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • A.K. Mittermaier, and L.E. Kay Observing biological dynamics at atomic resolution using NMR Trends Biochem. Sci. 34 2009 601 611
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 48
    • 59849106371 scopus 로고    scopus 로고
    • Protein promiscuity and its implications for biotechnology
    • I. Nobeli, A.D. Favia, and J.M. Thornton Protein promiscuity and its implications for biotechnology Nat. Biotechnol. 27 2009 157 167
    • (2009) Nat. Biotechnol. , vol.27 , pp. 157-167
    • Nobeli, I.1    Favia, A.D.2    Thornton, J.M.3
  • 49
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • A.G. Palmer 3rd, C.D. Kroenke, and J.P. Loria Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules Methods Enzymol. 339 2001 204 238
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 50
    • 59249094982 scopus 로고    scopus 로고
    • SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems
    • T. Panavas, C. Sanders, and T.R. Butt SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems Methods Mol. Biol. 497 2009 303 317
    • (2009) Methods Mol. Biol. , vol.497 , pp. 303-317
    • Panavas, T.1    Sanders, C.2    Butt, T.R.3
  • 51
    • 77957771797 scopus 로고    scopus 로고
    • Transient protein-protein interactions: Structural, functional, and network properties
    • J.R. Perkins, I. Diboun, B.H. Dessailly, J.G. Lees, and C. Orengo Transient protein-protein interactions: structural, functional, and network properties Structure 18 2010 1233 1243
    • (2010) Structure , vol.18 , pp. 1233-1243
    • Perkins, J.R.1    Diboun, I.2    Dessailly, B.H.3    Lees, J.G.4    Orengo, C.5
  • 52
    • 77950650685 scopus 로고    scopus 로고
    • Attenuated influenza virus vaccines with modified NS1 proteins
    • J.A. Richt, and A. García-Sastre Attenuated influenza virus vaccines with modified NS1 proteins Curr. Top. Microbiol. Immunol. 333 2009 177 195
    • (2009) Curr. Top. Microbiol. Immunol. , vol.333 , pp. 177-195
    • Richt, J.A.1    García-Sastre, A.2
  • 53
    • 0023151850 scopus 로고
    • Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli
    • G.S. Rule, E.A. Pratt, V. Simplaceanu, and C. Ho Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli Biochemistry 26 1987 549 556
    • (1987) Biochemistry , vol.26 , pp. 549-556
    • Rule, G.S.1    Pratt, E.A.2    Simplaceanu, V.3    Ho, C.4
  • 54
    • 69949085729 scopus 로고    scopus 로고
    • Independently inducible system of gene expression for condensed single protein production (cSPP) suitable for high efficiency isotope enrichment
    • W.M. Schneider, M. Inouye, G.T. Montelione, and M.J. Roth Independently inducible system of gene expression for condensed single protein production (cSPP) suitable for high efficiency isotope enrichment J. Struct. Funct. Genomics 10 2009 219 225
    • (2009) J. Struct. Funct. Genomics , vol.10 , pp. 219-225
    • Schneider, W.M.1    Inouye, M.2    Montelione, G.T.3    Roth, M.J.4
  • 55
  • 56
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • P. Schuck On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation Anal. Biochem. 320 2003 104 124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 57
    • 64849111005 scopus 로고    scopus 로고
    • Sending signals dynamically
    • R.G. Smock, and L.M. Gierasch Sending signals dynamically Science 324 2009 198 203
    • (2009) Science , vol.324 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 58
    • 33645792617 scopus 로고    scopus 로고
    • The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target
    • K.Y. Twu, D.L. Noah, P. Rao, R.L. Kuo, and R.M. Krug The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target J. Virol. 80 2006 3957 3965
    • (2006) J. Virol. , vol.80 , pp. 3957-3965
    • Twu, K.Y.1    Noah, D.L.2    Rao, P.3    Kuo, R.L.4    Krug, R.M.5
  • 60
    • 84864651001 scopus 로고    scopus 로고
    • Protein activity regulation by conformational entropy
    • S.R. Tzeng, and C.G. Kalodimos Protein activity regulation by conformational entropy Nature 488 2012 236 240
    • (2012) Nature , vol.488 , pp. 236-240
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 61
    • 34250177300 scopus 로고    scopus 로고
    • MatNMR: A flexible toolbox for processing, analyzing and visualizing magnetic resonance data in Matlab
    • J.D. van Beek matNMR: a flexible toolbox for processing, analyzing and visualizing magnetic resonance data in Matlab J. Magn. Reson. 187 2007 19 26
    • (2007) J. Magn. Reson. , vol.187 , pp. 19-26
    • Van Beek, J.D.1
  • 62
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • J. Vistica, J. Dam, A. Balbo, E. Yikilmaz, R.A. Mariuzza, T.A. Rouault, and P. Schuck Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition Anal. Biochem. 326 2004 234 256
    • (2004) Anal. Biochem. , vol.326 , pp. 234-256
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5    Rouault, T.A.6    Schuck, P.7
  • 63
    • 84873526287 scopus 로고    scopus 로고
    • The dark energy of proteins comes to light: Conformational entropy and its role in protein function revealed by NMR relaxation
    • A.J. Wand The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation Curr. Opin. Struct. Biol. 23 2013 75 81
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 75-81
    • Wand, A.J.1
  • 64
    • 0032995665 scopus 로고    scopus 로고
    • RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids
    • W. Wang, K. Riedel, P. Lynch, C.Y. Chien, G.T. Montelione, and R.M. Krug RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids RNA 5 1999 195 205
    • (1999) RNA , vol.5 , pp. 195-205
    • Wang, W.1    Riedel, K.2    Lynch, P.3    Chien, C.Y.4    Montelione, G.T.5    Krug, R.M.6
  • 67
    • 34547136235 scopus 로고    scopus 로고
    • Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses
    • C. Yin, J.A. Khan, G.V. Swapna, A. Ertekin, R.M. Krug, L. Tong, and G.T. Montelione Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses J. Biol. Chem. 282 2007 20584 20592
    • (2007) J. Biol. Chem. , vol.282 , pp. 20584-20592
    • Yin, C.1    Khan, J.A.2    Swapna, G.V.3    Ertekin, A.4    Krug, R.M.5    Tong, L.6    Montelione, G.T.7


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